Member database | PROSITE profiles |
PROSITE profiles type | domain |
Short name | S5_DSRBD |
Description
Ribosomal protein S5 is one of the proteins from the small ribosomal subunit.
In Escherichia coli, S5 is known to be important in the assembly and function
of the 30S ribosomal subunit. Mutations in S5 have been shown to increase
translational error frequencies.
The crystal structure of the S5 protein has been solved
[1] and consists of
two separated domains. An N-terminal domain which displays
some structurale homology to the dsRBD domain (alpha-beta(3)-alpha) and a mainly helical C-terminal domain that interacts with S8.
The dsRBD domain of the S5 protein interacts with the 16S RNA
[2].
S5 belongs to a family of ribosomal proteins which, on the basis of sequence
similarities [3,4], groups:
- Eubacterial S5.
- Cyanelle S5.
- Red algal chloroplast S5.
- Archaebacterial S5.
- Mammalian S2 (LLrep3).
- Caenorhabditis elegans S2 (C49H3.11).
- Drosophila S2.
- Plant S2.
- Yeast S4 (SUP44).
- Fungi mitochondrial S5.
S5 is a protein of 166 to 254 amino-acid residues. The signature pattern for
this protein is based on a conserved region, rich in glycine residues located
in the N-terminal domain. The profile we developed covers the entire
N-terminal dsRBD domain.
References
1.The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA. Ramakrishnan V, White SW. Nature 358, 768-71, (1992). View articlePMID: 1508272
2.Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA. Brodersen DE, Clemons WM Jr, Carter AP, Wimberly BT, Ramakrishnan V. J. Mol. Biol. 316, 725-68, (2002). View articlePMID: 11866529